Glycan repositioning of influenza hemagglutinin stem facilitates the elicitation of protective cross-group antibody responses - Boyoglu-Barnum, Seyhan; Hutchinson, Geoffrey B.; Boyington, Jeffrey C.; Moin, Syed M.; Gillespie, Rebecca A.; Tsybovsky, Yaroslav; Stephens, Tyler; Vaile, John R.; Lederhofer, Julia; Corbett, Kizzmekia S.; Fisher, Brian E.; Yassine, Hadi M.; et al. (Nature communications, 2020)
Keywords: 101/28; 13/1; 13/109; 631/250/2152/2153; 631/250/590; 631/326/596/1578; 631/45/612/1231; 64/60; 82/16; 82/83; Access control; Animals; Antibodies; Antibodies, Viral - immunology; Antibody Specificity; Asparagine - chemistry; Asparagine - metabolism; Broadly Neutralizing Antibodies - immunology; Cross Reactions; Epitopes; Epitopes - immunology; Female; Glycan; Glycosylation; Hemagglutinin Glycoproteins, Influenza Virus - chemistry; Hemagglutinin Glycoproteins, Influenza Virus - immunology; Hemagglutinin Glycoproteins, Influenza Virus - metabolism; Hemagglutinins; Humanities and Social Sciences; Immunoglobulins; Immunoglobulins - immunology; Influenza; Influenza A; Influenza A Virus, H7N9 Subtype - pathogenicity; Influenza Vaccines - immunology; Mice, Inbred BALB C; multidisciplinary; Nanoparticles; Nanoparticles - chemistry; Orthomyxoviridae Infections - immunology; Orthomyxoviridae Infections - prevention & control; Polysaccharides - chemistry; Science; Science (multidisciplinary); Vaccines; Viruses